Polysialylation promotes neural cell adhesion molecule-mediated cell migration in a fibroblast growth factor receptor-dependent manner, but independent of adhesion capability

被引：34

作者：

Li, Jing ^{[1
]}

Dai, Gong ^{[1
]}

Cheng, Ya-Bin ^{[1
]}

Qi, Xin ^{[1
]}

Geng, Mei-Yu ^{[1
,2
]}

机构：

[1] Ocean Univ China, Sch Med & Pharm, Dept Pharmacol & Glycobiol, Qingdao 266003, Peoples R China

[2] Chinese Acad Sci, Shanghai Inst Mat Med, Div Antitumor Pharmacol, State Key Lab Drug Res, Shanghai 201203, PR, Peoples R China

来源：

GLYCOBIOLOGY | 2011年 / 21卷 / 08期

关键词：

adhesion; FGFR; migration; NCAM; PSA; POLYSIALIC ACID EXPRESSION; BREAST-CANCER; NCAM; ACTIVATION; PATHWAYS; BINDING; STX;

D O I：

10.1093/glycob/cwr020

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Polysialic acid (PSA), a carbohydrate polymer mainly present in the neural cell adhesion molecule (NCAM), promotes neural plasticity; however, its mode of action in tumor malignancy remains largely unknown. In this study, we investigated the influence of polysialylation on cell migration. PSA consistently promoted cell migration on different extracellular matrices (ECMs) but differentially affected cell adhesion. All of these actions were reversed by endo-N-acetylneuraminidase treatment, and PSA-driven migration was inhibited by the specific fibroblast growth factor receptor (FGFR) inhibitor Su5402. Consistent with this latter observation, PSA-stimulated migration on different ECMs was paralleled by activation of the FGFR and its downstream signaling components, PLC-gamma, focal adhesion kinase and extracellular signal-regulated kinase 1/2. In contrast, the pattern of p59(fyn) activation correlated with differential adhesion to different ECMs. Collectively, these results indicate that PSA-conjugated NCAM potentiates signal transduction by the FGFR pathway and thereby enhances cell migration independent of adhesion capability, providing additional insights into the role of PSA in cancer development.

引用

页码：1010 / 1018

页数：9

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